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Originally published In Press as doi:10.1074/jbc.M010821200 on September 14, 2001

J. Biol. Chem., Vol. 276, Issue 47, 43723-43733, November 23, 2001
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NFkappa B-dependent Transcriptional Activation during Heat Shock Recovery
THERMOLABILITY OF THE NF-kappa B·Ikappa B COMPLEX*

Carole Kretz-Remy, Béatrice Munsch, and André-Patrick ArrigoDagger

From the Laboratoire Stress Oxydant, Chaperons, et Apoptose, Centre de Génétique Moléculaire et Cellulaire, CNRS-UMR 5534, Université Claude Bernard Lyon I, F-69622 Villeurbanne Cedex, France

Heat shock induces the accumulation of misfolded proteins and results in the preferential expression of heat shock proteins, which help the cell to recover from thermal damage. Heat shock is a well known transcriptional activator of the human immunodeficiency virus type 1 long terminal repeat (LTR). We report here that mutations or deletions of the LTR kappa B sites impaired the LTR transcriptional activation by heat shock. Further analysis revealed that, during heat shock recovery, the NF-kappa B p65 and p50 subunits migrated into the nucleus of HeLa cells, bound to DNA, and induced kappa B-dependent reporter gene expression. This NF-kappa B activation did not depend on new transcriptional and/or translational events and on the pro-oxidant state generated by heat shock. It was not concomitant with Ikappa Balpha phosphorylation and was not abolished by the expression of Ikappa B kinase or Ikappa Balpha dominant-negative mutants. Moreover, NF-kappa B activation and migration into the nucleus were not concomitant with Ikappa Balpha /beta or p105 degradation. However, during heat shock recovery, NF-kappa B was dissociated from its complexing partners, allowing its migration into the nucleus. Hence, we describe here a novel mechanism for activation of NF-kappa B based on the thermolability of the NF-kappa B·Ikappa B complex.

* This work was supported by Association pour la Recherche sur le Cancer Grant 5204 and by the Région Rhône-Alpes (to A.-P. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Lab. Stress Oxydant, Chaperons, et Apoptose, Centre de Génétique Moléculaire et Cellulaire, CNRS-UMR5534, Bâtiment Gregor Mendel, 16 rue Dubois, Université Claude Bernard Lyon I, F-69622 Villeurbanne Cedex, France. Tel.: 33-4-72-44-85-95; Fax: 33-4-72-44-05-55; E-mail: Arrigo@univ-lyon1.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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